Development and properties of recombinant proteins based on the broadly neutralizing antibody to influenza A virus

Алиев, Т. К.; Dement’yeva, I. G.; Toporova, V. A.; Bokov, M. N.; Pozdnyakova, L. P.; Рыбченко, В. С.; Долгих, Д. А.; Свешников, П. Г.; Kirpichnikov, Mikhaǐl P.

doi:10.3103/s0096392516020012

“…Western blotting confirmed previous results on the Fab-fragment of the FI6 IgG1-isotype antibody [13] indicating that antibody FI6 can interact with both whole HA0 hemagglutinin and the HA1 and HA2 fragments formed during hydrolysis of the whole protein in gel electrophoresis upon reducing conditions [21]. These results are consistent with the data of FI6 antibody epitope mapping presented in [8].…”

Section: Resultssupporting

confidence: 90%

The Development and Study of Recombinant Immunoglobulin A to Hemagglutinins of the Influenza Virus

Aliev¹,

Dement’yeva²,

Toporova³

et al. 2018

Acta Naturae

0

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We obtained recombinant variants of human antibody FI6 broadly specific to hemagglutinins of the influenza A virus. On the basis of a bi-promoter (CMV, hEF1-HTLV) vector, we developed genetic constructs for the expression of the heavy and light chains of the immunoglobulins of IgA1-, IgA2m1-, and IgG-isotypes. Following transfection and selection, stable Chinese hamster ovary (CHO) cell lines were produced. The antibodies of IgA1-, IgA2m1-, and IgG-isotypes were purified from culture media. We performed an immunochemical characterization and studied their interactions with influenza A strains of the H1N1- and H3N2-subtypes. It was shown that recombinant FI6 variants of the IgA-isotype retain the properties of the parental IgG antibody to demonstrate specificity to all the strains tested. The strongest binding was observed for the H1N1 subtype, which belongs to hemagglutinins of phylogenetic group I.

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“…Western blot data confirm the ability of the recombinant antibodies to recognize the native hemagglutinin of IAV. Western blotting confirmed previous results on the Fab-fragment of the FI6 IgG1-isotype antibody [ 13 ] indicating that antibody FI6 can interact with both whole HA0 hemagglutinin and the HA1 and HA2 fragments formed during hydrolysis of the whole protein in gel electrophoresis upon reducing conditions [ 21 ]. These results are consistent with the data of FI6 antibody epitope mapping presented in [ 8 ].…”

Section: Resultssupporting

confidence: 84%

“…We had previously synthesized [ 13 ] cDNA sequences of the variable domain of the heavy FI6VHv3 and light FI6VKv2 chains of antibody FI6 [ 8 ].…”

Section: Methodsmentioning

confidence: 99%

The Development and Study of Recombinant Immunoglobulin A to Hemagglutinins of the Influenza Virus

Алиев

¹

,

Dement’yeva

²

,

Toporova

³

et al. 2018

Acta Naturae

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1

0

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We obtained recombinant variants of human antibody FI6 broadly specific to hemagglutinins of the influenza A virus. On the basis of a bi-promoter (CMV, hEF1-HTLV) vector, we developed genetic constructs for the expression of the heavy and light chains of the immunoglobulins of IgA1-, IgA2m1-, and IgG-isotypes. Following transfection and selection, stable Chinese hamster ovary (CHO) cell lines were produced. The antibodies of IgA1-, IgA2m1-, and IgG-isotypes were purified from culture media. We performed an immunochemical characterization and studied their interactions with influenza A strains of the H1N1- and H3N2-subtypes. It was shown that recombinant FI6 variants of the IgA-isotype retain the properties of the parental IgG antibody to demonstrate specificity to all the strains tested. The strongest binding was observed for the H1N1 subtype, which belongs to hemagglutinins of phylogenetic group I.

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The Development and Inmmunochemical Properties of the Dimer of Immunoglobulin A Specific to the Influenza Virus A Hemagglutinin

Алиев

¹

,

Дементьева

²

,

Toporova

³

et al. 2018

Dokl Biochem Biophys

0

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We obtained dimeric forms of IgA1- and IgA2m1-isotypes of FI6 antibody broadly specific to hemagglutinins of different subtypes of influenza A virus. It was shown that the dimers of IgA1 isotype are characterized by a higher antigen-binding activity compared to the IgA2m1 dimers. The affinity of IgA1 dimers to the strains of the H1N1 subtype is higher than that of the H3N2 subtype, which correlates with the properties of the parental human FI6 antibody.

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Development and properties of recombinant proteins based on the broadly neutralizing antibody to influenza A virus

Cited by 4 publications

References 11 publications

The Development and Study of Recombinant Immunoglobulin A to Hemagglutinins of the Influenza Virus

The Development and Study of Recombinant Immunoglobulin A to Hemagglutinins of the Influenza Virus

The Development and Study of Recombinant Immunoglobulin A to Hemagglutinins of the Influenza Virus

The Development and Inmmunochemical Properties of the Dimer of Immunoglobulin A Specific to the Influenza Virus A Hemagglutinin

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